Interacting Partners for Kringle Domains Of Plasminogen: Common Binding With K1 and K5 Domains
Authors: Kong, Naehyun; Lim, Dongyeol; Lee, Kyunghee
Source: Protein and Peptide Letters, Volume 11, Number 6, December 2004 , pp. 521-525(5)
Publisher: Bentham Science Publishers
Abstract:We have identified MAZR and Rgl2 as specific interacting partners for kringle domains in angiostatin (K1-4) and K5 using yeast two hybrid screening. Both K1 and K1-4 have strong interaction with MAZR and Rgl2 whereas K5 only binds with Rgl2. No interaction of K2, K3, and K4 with either of these binding proteins was detected. We suggest that a common binding motif may exist near LBS-4 that is required for binding with Rgl2 but not with MAZR.
Document Type: Review Article
Affiliations: Department of Applied Chemistry, Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul 143-747, South Korea.
Publication date: December 1, 2004
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.